SCOP 1.63: Domain d1mh3a2: 1mh3 A:1-366

Lineage for d1mh3a2 (1mh3 A:1-366)

1. Root: SCOP 1.63

2. Class c: Alpha and beta proteins (a/b) [51349] (117 folds)

3. Fold c.94: Periplasmic binding protein-like II [53849] (1 superfamily)
   consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication
   mixed beta-sheet of 5 strands, order 21354; strand 5 is antiparallel to the rest

4. Superfamily c.94.1: Periplasmic binding protein-like II [53850] (2 families)
   Similar in architecture to the superfamily I but partly differs in topology

5. Family c.94.1.1: Phosphate binding protein-like [53851] (19 proteins)

6. Protein D-maltodextrin-binding protein, MBP [53862] (3 species)
   contains a few additional helices in the C-terminal extension; homologous to thiaminase I

7. Species Escherichia coli [TaxId:562] [53863] (29 PDB entries)

8. Domain d1mh3a2: 1mh3 A:1-366 [79113]
   Other proteins in same PDB: d1mh3a1
   chimera with yeast a1 homeodomain
   mutant

Details for d1mh3a2

PDB Entry: 1mh3, 2.1 Å

PDB Description: maltose binding-a1 homeodomain protein chimera, crystal form i

SCOP Domain Sequences for d1mh3a2:

Sequence; same for both SEQRES and ATOM records:

>d1mh3a2 c.94.1.1 (A:1-366) D-maltodextrin-binding protein, MBP {Escherichia coli}
kieegklviwingdkgynglaevgkkfekdtgikvtvehpdkleekfpqvaatgdgpdii
fwahdrfggyaqsgllaeitpdkafqdklypftwdavryngkliaypiavealsliynkd
llpnppktweeipaldkelkakgksalmfnlqepyftwpliaadggyafkyengkydikd
vgvdnagakagltflvdliknkhmnadtdysiaeaafnkgetamtingpwawsnidtskv
nygvtvlptfkgqpskpfvgvlsaginaaspnkelakeflenylltdegleavnkdkplg
avalksyeeelakdpriaatmenaqkgeimpnipqmsafwyavrtavinaasgrqtvdaa
laaaqt

Timeline for d1mh3a2:

• d1mh3a2 is new in SCOP 1.63
  
• d1mh3a2 appears in SCOP 1.65
  
• d1mh3a2 appears in the current release, SCOPe 2.08